ArticleBiochimica et biophysica acta. Bioenergetics2020
Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix.
Article in Biochimica et biophysica acta. Bioenergetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Two-Photon-Driven Photoprotection Mechanism in Echinenone-Functionalized Orange Carotenoid Protein.Journal of the American Chemical Society · 2025Article
- Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis.Protein science : a publication of the Protein Society · 2024Review
- The Orange Carotenoid Protein Triggers Cyanobacterial Photoprotection by Quenching Bilins via a Structural Switch of Its Carotenoid.Journal of the American Chemical Society · 2024Article
- Color-Tuning Mechanism of the Lit Form of Orange Carotenoid Protein.Molecules and cells · 2023Article
- Is orange carotenoid protein photoactivation a single-photon process?Biophysical reports · 2022Article
- Article
- A synthetic switch based on orange carotenoid protein to control blue-green light responses in chloroplasts.Plant physiology · 2022Article
- Unifying Perspective of the Ultrafast Photodynamics of Orange Carotenoid Proteins fromJACS Au · 2022Article
- Integrated Structural Studies for Elucidating Carotenoid-Protein Interactions.Advances in experimental medicine and biology · 2022Article
- Role of hydrogen bond alternation and charge transfer states in photoactivation of the Orange Carotenoid Protein.Communications biology · 2021Article
- Environmental Tuning of Homologs of the Orange Carotenoid Protein-Encoding Gene in the CyanobacteriumFrontiers in microbiology · 2021Article
- Probing of carotenoid-tryptophan hydrogen bonding dynamics in the single-tryptophan photoactive Orange Carotenoid Protein.Scientific reports · 2020Article
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13 authors.
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Abstract
The orange carotenoid protein (OCP) is a structurally and functionally modular photoactive protein involved in cyanobacterial photoprotection. Recently, based on bioinformatic analysis and phylogenetic relationships, new families of OCP have been described, OCP2 and OCPx. The first characterization of the OCP2 showed both faster photoconversion and back-conversion, and lower fluorescence quenching of phycobilisomes relative to the well-characterized OCP1. Moreover, OCP2 is not regulated by the fluorescence recovery protein (FRP). In this work, we present a comprehensive study combining ultrafast spectroscopy and structural analysis to compare the photoactivation mechanisms of OCP1 and OCP2 from Tolypothrix PCC 7601. We show that despite significant differences in their functional characteristics, the spectroscopic properties of OCP1 and OCP2 are comparable. This indicates that the OCP functionality is not directly related to the spectroscopic properties of the bound carotenoid. In addition, the structural analysis by X-ray footprinting reveals that, overall, OCP1 and OCP2 have grossly the same photoactivation mechanism. However, the OCP2 is less reactive to radiolytic labeling, suggesting that the protein is less flexible than OCP1. This observation could explain fast photoconversion of OCP2.
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